Protein profiling of Guillain–Barrè syndrome cerebrospinal fluid by two-dimensional electrophoresis and mass spectrometry

Protein profiling of cerebrospinal fluid in Guillain–Barrè syndrome (GBS), an acute and immune-mediated disease affecting the peripheral nervous system, was performed by two-dimensional electrophoresis. Significant modulated spots in GBS patients vs. control groups (a group of multiple sclerosis patients and one of healthy donors) underwent MALDI-TOF/TOF investigation. Inflammation-related proteins, such as vitamin D-binding protein, beta-2 glycoprotein I (ApoH), and a complement component C3 isoform were up-regulated in GBS, whereas transthyretin (the monomer and the dimer forms), apolipoprotein E, albumin and five of its fragments were down-regulated. Then, we used an isoelectric-focusing-dinitrophenylhydrazine-based technique to analyse the extent of carbonylation and, as a result, of oxidative damage of GBS CSF proteome. We observed a major sensitivity to carbonylation for albumin and alpha-glycoprotein in inflammation and a selective increase of reactivity for a glycosylated Fab from an IgM globulin in GBS CSF. Our results add new proteins to candidate CSF features of GBS, and suggest that oxidative stress could contribute to the immunopathological mechanisms in this syndrome.

Research highlights▶ Inflammation-related proteins were up-regulated in CSF of GBS. ▶Both the monomer and the dimer forms of TTR were down-regulated in CSF of GBS. ▶ Apo E, albumin and five of its fragments were down-regulated in CSF of GBS. ▶ A glycosylated Fab from an IgM globulin was high carbonylated in GBS CSF.